Characterization of a G-protein-regulated outward K+ current in mesophyll cells of Vicia faba L
Whole-cell voltage-dependent currents in isolated mesophyll protoplasts of Vicia faba were investigated by patch-clamp techniques. With 104 millimole K+ in the cytosol and 13 millimole K+ in the external solution, depolarization of the plasma membrane from -47 mV to potentials between -15 and +85 mV...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1993-01, Vol.90 (1), p.262-266 |
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| creator | Li, W.W. (Harvard University, Cambridge, MA) Assmann, S.M |
| description | Whole-cell voltage-dependent currents in isolated mesophyll protoplasts of Vicia faba were investigated by patch-clamp techniques. With 104 millimole K+ in the cytosol and 13 millimole K+ in the external solution, depolarization of the plasma membrane from -47 mV to potentials between -15 and +85 mV activated a voltage- and time-dependent outward current (I out). The average magnitude of I out at +85 mV was 28.5 +/- 3.3 pA.pF-1. No inward voltage-dependent current was observed upon hyperpolarization of the plasma membrane from -55 mV to potentials as negative as -175 mV. Time-activated out-ward current was blocked by Ba2+ (1 millimole BaC12) and was not observed when K+ was eliminated from the external and internal solutions, indicating that this outward current was carried primarily by K+ ions. The voltage dependency of outward K+ current revealed a possible mechanism for K+ efflux from mesophyll cells. A GDP analogue guanosine 5'-[beta-thio]diphosphate (500 millimole) significantly enhanced outward K+ current. The outward K+ current was inhibited by the GTP analogue guanosine 5'-[gamma-thio](triphosphate (500 micromolar) and by an increase in cytoplasmic free Ca2+ concentrations. Cholera toxin, which ADP-ribosylates guanine nucleotide-binding regulatory proteins, also inhibited outward K+ current. These findings illustrate the presence in mesophyll cells of outward rectifying K+ channels that are regulated by GTP-binding proteins and calcium |
| doi_str_mv | 10.1073/pnas.90.1.262 |
| format | Article |
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(Harvard University, Cambridge, MA) ; Assmann, S.M</creator><creatorcontrib>Li, W.W. (Harvard University, Cambridge, MA) ; Assmann, S.M</creatorcontrib><description>Whole-cell voltage-dependent currents in isolated mesophyll protoplasts of Vicia faba were investigated by patch-clamp techniques. With 104 millimole K+ in the cytosol and 13 millimole K+ in the external solution, depolarization of the plasma membrane from -47 mV to potentials between -15 and +85 mV activated a voltage- and time-dependent outward current (I out). The average magnitude of I out at +85 mV was 28.5 +/- 3.3 pA.pF-1. No inward voltage-dependent current was observed upon hyperpolarization of the plasma membrane from -55 mV to potentials as negative as -175 mV. Time-activated out-ward current was blocked by Ba2+ (1 millimole BaC12) and was not observed when K+ was eliminated from the external and internal solutions, indicating that this outward current was carried primarily by K+ ions. The voltage dependency of outward K+ current revealed a possible mechanism for K+ efflux from mesophyll cells. A GDP analogue guanosine 5'-[beta-thio]diphosphate (500 millimole) significantly enhanced outward K+ current. The outward K+ current was inhibited by the GTP analogue guanosine 5'-[gamma-thio](triphosphate (500 micromolar) and by an increase in cytoplasmic free Ca2+ concentrations. Cholera toxin, which ADP-ribosylates guanine nucleotide-binding regulatory proteins, also inhibited outward K+ current. These findings illustrate the presence in mesophyll cells of outward rectifying K+ channels that are regulated by GTP-binding proteins and calcium</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.90.1.262</identifier><identifier>PMID: 8419932</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Adenosine Diphosphate - analogs & derivatives ; Adenosine Diphosphate - pharmacology ; Biological and medical sciences ; Biology ; CATION ; CATIONES ; Cell Membrane - physiology ; Cell membranes ; Cell physiology ; Cholera Toxin - pharmacology ; Egtazic Acid - analogs & derivatives ; Egtazic Acid - pharmacology ; Electric current ; Electric potential ; Electric Stimulation ; Flowers & plants ; Fundamental and applied biological sciences. Psychology ; GTP-Binding Proteins - physiology ; Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology ; Guanosine Diphosphate - analogs & derivatives ; Guanosine Diphosphate - pharmacology ; Guard cells ; Membrane and intracellular transports ; Membrane potential ; Membrane Potentials - drug effects ; MESOFILO ; Mesophyll ; Mesophyll cells ; MESOPHYLLE ; Molecular and cellular biology ; Pertussis Toxin ; Plant Cells ; Plant Physiological Phenomena ; Plasma currents ; POTASIO ; POTASSIUM ; Potassium Channels - drug effects ; Potassium Channels - physiology ; Proteins ; PROTOPLASMA ; PROTOPLASME ; Protoplasts ; Protoplasts - physiology ; Thionucleotides - pharmacology ; VICIA FABA ; Virulence Factors, Bordetella - pharmacology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1993-01, Vol.90 (1), p.262-266</ispartof><rights>Copyright 1993 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Jan 1, 1993</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c593t-9e8000ffee266d187367f150b5e561391d0f4c52fc48e65c0e2198065c9024c23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/90/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2361030$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2361030$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,4025,27928,27929,27930,53796,53798,58022,58255</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4639575$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8419932$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, W.W. (Harvard University, Cambridge, MA)</creatorcontrib><creatorcontrib>Assmann, S.M</creatorcontrib><title>Characterization of a G-protein-regulated outward K+ current in mesophyll cells of Vicia faba L</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Whole-cell voltage-dependent currents in isolated mesophyll protoplasts of Vicia faba were investigated by patch-clamp techniques. With 104 millimole K+ in the cytosol and 13 millimole K+ in the external solution, depolarization of the plasma membrane from -47 mV to potentials between -15 and +85 mV activated a voltage- and time-dependent outward current (I out). The average magnitude of I out at +85 mV was 28.5 +/- 3.3 pA.pF-1. No inward voltage-dependent current was observed upon hyperpolarization of the plasma membrane from -55 mV to potentials as negative as -175 mV. Time-activated out-ward current was blocked by Ba2+ (1 millimole BaC12) and was not observed when K+ was eliminated from the external and internal solutions, indicating that this outward current was carried primarily by K+ ions. The voltage dependency of outward K+ current revealed a possible mechanism for K+ efflux from mesophyll cells. A GDP analogue guanosine 5'-[beta-thio]diphosphate (500 millimole) significantly enhanced outward K+ current. The outward K+ current was inhibited by the GTP analogue guanosine 5'-[gamma-thio](triphosphate (500 micromolar) and by an increase in cytoplasmic free Ca2+ concentrations. Cholera toxin, which ADP-ribosylates guanine nucleotide-binding regulatory proteins, also inhibited outward K+ current. These findings illustrate the presence in mesophyll cells of outward rectifying K+ channels that are regulated by GTP-binding proteins and calcium</description><subject>Adenosine Diphosphate - analogs & derivatives</subject><subject>Adenosine Diphosphate - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Biology</subject><subject>CATION</subject><subject>CATIONES</subject><subject>Cell Membrane - physiology</subject><subject>Cell membranes</subject><subject>Cell physiology</subject><subject>Cholera Toxin - pharmacology</subject><subject>Egtazic Acid - analogs & derivatives</subject><subject>Egtazic Acid - pharmacology</subject><subject>Electric current</subject><subject>Electric potential</subject><subject>Electric Stimulation</subject><subject>Flowers & plants</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GTP-Binding Proteins - physiology</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</subject><subject>Guanosine Diphosphate - analogs & derivatives</subject><subject>Guanosine Diphosphate - pharmacology</subject><subject>Guard cells</subject><subject>Membrane and intracellular transports</subject><subject>Membrane potential</subject><subject>Membrane Potentials - drug effects</subject><subject>MESOFILO</subject><subject>Mesophyll</subject><subject>Mesophyll cells</subject><subject>MESOPHYLLE</subject><subject>Molecular and cellular biology</subject><subject>Pertussis Toxin</subject><subject>Plant Cells</subject><subject>Plant Physiological Phenomena</subject><subject>Plasma currents</subject><subject>POTASIO</subject><subject>POTASSIUM</subject><subject>Potassium Channels - drug effects</subject><subject>Potassium Channels - physiology</subject><subject>Proteins</subject><subject>PROTOPLASMA</subject><subject>PROTOPLASME</subject><subject>Protoplasts</subject><subject>Protoplasts - physiology</subject><subject>Thionucleotides - pharmacology</subject><subject>VICIA FABA</subject><subject>Virulence Factors, Bordetella - pharmacology</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc-LEzEUxwdR1rp69CIKQdaTTM3vmYAXKe4qFjzoeg1pJmlT0slsklHXv94Mna168ZSEz-e9fHmvqp4iuESwIW-GXqWlKI8l5vhetUBQoJpTAe9XCwhxU7cU04fVo5T2EELBWnhWnbUUCUHwopKrnYpKZxPdL5Vd6EGwQIGreoghG9fX0WxHr7LpQBjzDxU78Ok10GOMps_A9eBgUhh2t94DbbxPU_k3p50CVm0UWD-uHljlk3kyn-fV9eX7r6sP9frz1cfVu3WtmSC5FqYt4aw1BnPeobYhvLGIwQ0zjCMiUAct1QxbTVvDmYYGI9HCchMQU43JefX22HcYNwfT6ZIuKi-H6A4q3sqgnPyX9G4nt-G7pIxTWMpfzuUx3IwmZbkPY-xLYokhwi1pBSpSfZR0DClFY0_tEZTTLuS0CynKQ5ZdFP_F35lO9jz8wi9mrpJW3kbVa5dOGuVEsIYV7dWsTd3v6N0v0o7eZ_MzF-_5f7w_eJ9yiCeOCUeQTBN4dsRWBam2sQS5_iIIwUJA8hu3Vbpc</recordid><startdate>19930101</startdate><enddate>19930101</enddate><creator>Li, W.W. (Harvard University, Cambridge, MA)</creator><creator>Assmann, S.M</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19930101</creationdate><title>Characterization of a G-protein-regulated outward K+ current in mesophyll cells of Vicia faba L</title><author>Li, W.W. (Harvard University, Cambridge, MA) ; Assmann, S.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c593t-9e8000ffee266d187367f150b5e561391d0f4c52fc48e65c0e2198065c9024c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Adenosine Diphosphate - analogs & derivatives</topic><topic>Adenosine Diphosphate - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Biology</topic><topic>CATION</topic><topic>CATIONES</topic><topic>Cell Membrane - physiology</topic><topic>Cell membranes</topic><topic>Cell physiology</topic><topic>Cholera Toxin - pharmacology</topic><topic>Egtazic Acid - analogs & derivatives</topic><topic>Egtazic Acid - pharmacology</topic><topic>Electric current</topic><topic>Electric potential</topic><topic>Electric Stimulation</topic><topic>Flowers & plants</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GTP-Binding Proteins - physiology</topic><topic>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</topic><topic>Guanosine Diphosphate - analogs & derivatives</topic><topic>Guanosine Diphosphate - pharmacology</topic><topic>Guard cells</topic><topic>Membrane and intracellular transports</topic><topic>Membrane potential</topic><topic>Membrane Potentials - drug effects</topic><topic>MESOFILO</topic><topic>Mesophyll</topic><topic>Mesophyll cells</topic><topic>MESOPHYLLE</topic><topic>Molecular and cellular biology</topic><topic>Pertussis Toxin</topic><topic>Plant Cells</topic><topic>Plant Physiological Phenomena</topic><topic>Plasma currents</topic><topic>POTASIO</topic><topic>POTASSIUM</topic><topic>Potassium Channels - drug effects</topic><topic>Potassium Channels - physiology</topic><topic>Proteins</topic><topic>PROTOPLASMA</topic><topic>PROTOPLASME</topic><topic>Protoplasts</topic><topic>Protoplasts - physiology</topic><topic>Thionucleotides - pharmacology</topic><topic>VICIA FABA</topic><topic>Virulence Factors, Bordetella - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, W.W. 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(Harvard University, Cambridge, MA)</au><au>Assmann, S.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a G-protein-regulated outward K+ current in mesophyll cells of Vicia faba L</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1993-01-01</date><risdate>1993</risdate><volume>90</volume><issue>1</issue><spage>262</spage><epage>266</epage><pages>262-266</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Whole-cell voltage-dependent currents in isolated mesophyll protoplasts of Vicia faba were investigated by patch-clamp techniques. With 104 millimole K+ in the cytosol and 13 millimole K+ in the external solution, depolarization of the plasma membrane from -47 mV to potentials between -15 and +85 mV activated a voltage- and time-dependent outward current (I out). The average magnitude of I out at +85 mV was 28.5 +/- 3.3 pA.pF-1. No inward voltage-dependent current was observed upon hyperpolarization of the plasma membrane from -55 mV to potentials as negative as -175 mV. Time-activated out-ward current was blocked by Ba2+ (1 millimole BaC12) and was not observed when K+ was eliminated from the external and internal solutions, indicating that this outward current was carried primarily by K+ ions. The voltage dependency of outward K+ current revealed a possible mechanism for K+ efflux from mesophyll cells. A GDP analogue guanosine 5'-[beta-thio]diphosphate (500 millimole) significantly enhanced outward K+ current. The outward K+ current was inhibited by the GTP analogue guanosine 5'-[gamma-thio](triphosphate (500 micromolar) and by an increase in cytoplasmic free Ca2+ concentrations. Cholera toxin, which ADP-ribosylates guanine nucleotide-binding regulatory proteins, also inhibited outward K+ current. These findings illustrate the presence in mesophyll cells of outward rectifying K+ channels that are regulated by GTP-binding proteins and calcium</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8419932</pmid><doi>10.1073/pnas.90.1.262</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0027-8424 1091-6490 |
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| recordid | cdi_pascalfrancis_primary_4639575 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Diphosphate - analogs & derivatives Adenosine Diphosphate - pharmacology Biological and medical sciences Biology CATION CATIONES Cell Membrane - physiology Cell membranes Cell physiology Cholera Toxin - pharmacology Egtazic Acid - analogs & derivatives Egtazic Acid - pharmacology Electric current Electric potential Electric Stimulation Flowers & plants Fundamental and applied biological sciences. Psychology GTP-Binding Proteins - physiology Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology Guanosine Diphosphate - analogs & derivatives Guanosine Diphosphate - pharmacology Guard cells Membrane and intracellular transports Membrane potential Membrane Potentials - drug effects MESOFILO Mesophyll Mesophyll cells MESOPHYLLE Molecular and cellular biology Pertussis Toxin Plant Cells Plant Physiological Phenomena Plasma currents POTASIO POTASSIUM Potassium Channels - drug effects Potassium Channels - physiology Proteins PROTOPLASMA PROTOPLASME Protoplasts Protoplasts - physiology Thionucleotides - pharmacology VICIA FABA Virulence Factors, Bordetella - pharmacology |
| title | Characterization of a G-protein-regulated outward K+ current in mesophyll cells of Vicia faba L |
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